The collaboration with the Gierasch research group at the University of Massachusetts is essential for both studying peptides by solid-state NMR spectroscopy and the development of the spectroscopy. During the past year the availability of a variety of backbone and sidechain labeled amino acids and peptides has enabled the multidimensional experiments to be used to characterize the 1H chemical shift, 1H-15N dipolar, and 15N chemical shift tensors at key sites, including several different peptide linkages and both Trp and His sidechains. The magnitudes and orientations of the principal values of the various tensors are essential information for the determination of the structures of oriented proteins and other spectroscopic experiments.